Number of the records: 1

Saccharomyces cerevisiae can secrete Sapp1p proteinase of Candida parapsilosis but cannot use it for efficient nitrogen acquisition

SYSNO ASEP	0394743
Document Type	J - Journal Article
R&D Document Type	Journal Article
Subsidiary J	Článek ve WOS
Title	Saccharomyces cerevisiae can secrete Sapp1p proteinase of Candida parapsilosis but cannot use it for efficient nitrogen acquisition
Author(s)	Vinterová, Zuzana (UOCHB-X) Bauerová, Václava (UOCHB-X) Dostál, Jiří (UOCHB-X)_{RID, ORCID} Sychrová, Hana (FGU-C)_{RID, ORCID} Hrušková-Heidingsfeldová, Olga (UOCHB-X)_{RID, ORCID} Pichová, Iva (UOCHB-X)_{RID, ORCID}
Number of authors	6
Source Title	Journal of Microbiology. - : Microbiological society of Korea - ISSN 1225-8873 Roč. 51, č. 3 (2013), s. 336-344
Number of pages	9 s.
Language	eng - English
Country	KR - Korea, Republic of
Keywords	Candida parapsilosis ; Saccharomyces cerevisiae ; secreted aspartic proteinase ; SAPP1 ; nitrogen metabolism
Subject RIV	EE - Microbiology, Virology
Subject RIV - cooperation	Institute of Physiology - Microbiology, Virology
R&D Projects	GA310/09/1945 GA ČR - Czech Science Foundation (CSF)
	GAP302/12/1151 GA ČR - Czech Science Foundation (CSF)
Institutional support	UOCHB-X - RVO:61388963 ; FGU-C - RVO:67985823
UT WOS	000321134100011
EID SCOPUS	84879612563
DOI	10.1007/s12275-013-2422-4
Annotation	Secreted aspartic proteinase Sapp1p of Candida parapsilosis represents one of the factors contributing to the pathogenicity of the fungus. The proteinase is synthesized as an inactive pre-pro-enzyme, but only processed Sapp1p is secreted into extracellular space. We constructed a plasmid containing the SAPP1 coding sequence under control of the ScGAL1 promoter and used it for proteinase expression in a Saccharomyces cerevisiae kex2 Delta mutant. Because Sapp1p maturation depends on cleavage by Kex2p proteinase, the kex2 Delta mutant secreted only the pro-form of Sapp1p. Characterization of this secreted proteinase form revealed that the Sapp1p signal peptide consists of 23 amino acids. Additionally, we prepared a plasmid with the SAPP1 coding sequence under control of its authentic CpSAPP1 promoter, which contains two GATAA motifs. While in C. parapsilosis SAPP1 expression is repressed by good low molecular weight nitrogen sources (e.g., ammonium ions), S. cerevisiae cells harboring this plasmid secreted a low concentration of active proteinase regardless of the type of nitrogen source used. Quantitative real-time PCR analysis of a set of genes related to nitrogen metabolism and uptake (GAT1, GLN3, STP2, GAP1, OPT1, and PTR2) obtained from S. cerevisiae cells transformed with either plasmid encoding SAPP1 under control of its own promoter or empty vector and cultivated in media containing various nitrogen sources also suggested that SAPP1 expression can be connected with the S. cerevisiae regulatory network. However, this regulation occurs in a different manner than in C. parapsilosis.
Workplace	Institute of Organic Chemistry and Biochemistry
Contact	asep@uochb.cas.cz ; Kateřina Šperková, Tel.: 232 002 584 ; Viktorie Chládková, Tel.: 232 002 434
Year of Publishing	2014

Number of the records: 1